ID A0A1Q5N4G5_9ACTN Unreviewed; 368 AA.
AC A0A1Q5N4G5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OKK21343.1};
GN ORFNames=AMK09_12715 {ECO:0000313|EMBL:OKK21343.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK21343.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK21343.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK21343.1,
RC ECO:0000313|Proteomes:UP000186200};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKK21343.1}.
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DR EMBL; LIVO01000004; OKK21343.1; -; Genomic_DNA.
DR RefSeq; WP_073734837.1; NZ_LIVO01000004.1.
DR AlphaFoldDB; A0A1Q5N4G5; -.
DR STRING; 1703920.AMK09_12715; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000186200; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186200};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..367
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 368 AA; 38152 MW; 3EB34A2A67C08756 CRC64;
MTNVTAAVAR ERTARLNLEQ LRLDEIRDNE VRVRMVASGI CHADALTRDG VYPTPQPAVL
GHEGAGVVES VGRAVSRVRA GDRVVLSAAY CTNCVQCLAG HTAYCENLFA EDFGGRRGDG
STALSTQDGE TVSSHFFGQS SFSTYANVVE SSVVPVSASA PLETLAPLGC GMQTGAGAVL
NDLRPPVGSS FAVTGAGAVG LAAIMAARVA GCSTVIAVDL HDSRLDLAKE LGATHTVNSR
GGDVPAELMR ITGGKGVNYI LDTTAVPAVL GALPQALAVR GTLALVGSAP AGTEVPFEIG
ASLPKGWTFK TIIQGGAVPQ LFIPRMVDLW EQGRFPFDKL IKHYAFADIN TAFADSASGA
TVKPVVLF
//
